Zinc in PDB 1e4a: L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant Del(27)

All present enzymatic activity of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant Del(27):
4.1.2.17;

The structure of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant Del(27), PDB code: 1e4a was solved by A.C.Joerger, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.15
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.250, 93.250, 43.400, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 22.3

The binding sites of Zinc atom in the L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant Del(27) (pdb code 1e4a). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant Del(27), PDB code: 1e4a:

Zinc binding site 1 out of 1 in the L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant Del(27)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant Del(27) within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn304 b:12.9 occ:1.00 OE2 P:GLU73 2.0 16.2 1.0 NE2 P:HIS155 2.1 9.3 1.0 NE2 P:HIS94 2.1 15.6 1.0 NE2 P:HIS92 2.2 11.2 1.0 OE1 P:GLU73 2.5 17.8 1.0 CD P:GLU73 2.6 16.3 1.0 CD2 P:HIS155 3.0 9.8 1.0 CD2 P:HIS94 3.0 15.8 1.0 CD2 P:HIS92 3.1 10.3 1.0 CE1 P:HIS155 3.1 10.9 1.0 CE1 P:HIS92 3.2 9.8 1.0 CE1 P:HIS94 3.2 17.2 1.0 O P:HOH409 3.8 33.5 1.0 CG P:GLU73 4.1 15.1 1.0 CG P:HIS155 4.2 9.9 1.0 ND1 P:HIS155 4.2 11.3 1.0 CG P:HIS94 4.2 16.4 1.0 CG P:HIS92 4.2 9.1 1.0 ND1 P:HIS92 4.3 9.8 1.0 ND1 P:HIS94 4.3 16.2 1.0 CZ P:PHE76 4.6 17.2 1.0 O P:THR26 4.9 47.1 1.0 CB P:GLU73 5.0 16.4 1.0 ND2 P:ASN29 5.0 11.4 1.0

A.C.Joerger, C.Mueller-Dieckmann, G.E.Schulz. Structures of L-Fuculose-1-Phosphate Aldolase Mutants Outlining Motions During Catalysis J.Mol.Biol. V. 303 531 2000.
ISSN: ISSN 0022-2836
PubMed: 11054289
DOI: 10.1006/JMBI.2000.4153